| Autor: |
Taby O; Centre National de Transfusion Sanguine, Les Ulis, France., Chabbat J, Steinbuch M |
| Jazyk: |
angličtina |
| Zdroj: |
Thrombosis research [Thromb Res] 1990 Jul 01; Vol. 59 (1), pp. 27-35. |
| DOI: |
10.1016/0049-3848(90)90268-h |
| Abstrakt: |
The study of the interaction between activated protein C (APC) and non-plasmatic inhibitors allowed us to demonstrate that aprotinin is a potent competitive inhibitor of APC with a Ki of 1.35 mumol/L. It was possible to adsorb immunopurified protein C (PC) activated by venom activator to insolubilized aprotinin and to recover the active enzyme after elution by HCl 0.1 N or by a chaotropic ion, for example KSCN 3 mol/L. The interaction involved the active-site of the enzyme since PC and DIP-APC did not bind to the matrix. Thus, APC could be purified, after activation, in a one-stage procedure out of a mixture of protein such as a prothrombin complex concentrate. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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